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Search term: Rv1438

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nametpi
Rv numberRv1438
TypeCDS
FunctionPlays an important role in several metabolic pathways [catalytic activity: D-glyceraldehyde 3-phosphate = glycerone phosphate]
ProductProbable triosephosphate isomerase Tpi (TIM)
CommentsRv1438, (MTCY493.16c), len: 261 aa. Probable tpi (tpiA), Triosephosphate isomerase, highly similar to many e.g. TPIS_MYCLE|P46711 Mycobacterium leprae (261 aa), FASTA scores: opt: 1456, E(): 0, (83.9% identity in 261 aa overlap). Contains PS00171 Triosephosphate isomerase active site. Belongs to the triosephosphate isomerase family.
Molecular mass (Da)27371
Isoelectric point5.7878
Gene length (bp)786
Protein length261
Location (kb)1615.56


Functional categoryintermediary metabolism and respiration


ProteomicsThe product of this CDS corresponds to spot 3_302 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see citations below). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified in the cytosol of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website


Coordinates
TypeStartEndOrientation
RBS16155551615559+
CDS16155641616349+


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1438|tpi
VSRKPLIAGNWKMNLNHYEAIALVQKIAFSLPDKYYDRVDVAVIPPFTDLRSVQTLVDGD
KLRLTYGAQDLSPHDSGAYTGDVSGAFLAKLGCSYVVVGHSERRTYHNEDDALVAAKAAT
ALKHGLTPIVCIGEHLDVREAGNHVAHNIEQLRGSLAGLLAEQIGSVVIAYEPVWAIGTG
RVASAADAQEVCAAIRKELASLASPRIADTVRVLYGGSVNAKNVGDIVAQDDVDGGLVGG
ASLDGEHFATLAAIAAGGPLP
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
PFAMP66940
Protein Data Bank3GVG 3TA6 3TAO


Orthologs/Cross-references
CDC1551MT1482
Enzyme Classification5.3.1.1
Gene Ontologytriose-phosphate isomerase activity
cytoplasm
gluconeogenesis
glycolysis
pentose-phosphate shunt
M. bovisMb1473
M. lepraeML0572
M. marinumMMAR_2241
M. smegmatisMSMEG_3086
UniProtP66940
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv1438


Expression Data
TBDBRv1438


Bibliography
Mollenkopf HJ, Jungblut PR, Raupach B, Mattow J, Lamer S, Zimny-Arndt U, Zimny -Arndt U, Schaible UE, Kaufmann SH,
A dynamic two-dimensional polyacrylamide gel electrophoresis database: the mycobacterial proteome via Internet
Electrophoresis (1999) 20(11):2172-80
Cited for: Proteomics
Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Zimny -Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K, Kaufmann SH,
Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens
Mol Microbiol (1999) 33(6):1103-17
Cited for: Proteomics
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Cited for: Proteomics
Mattow J, Schaible UE, Schmidt F, Hagens K, Siejak F, Brestrich G, Haeselbarth G, Muller EC, Jungblut PR, Kaufmann SH,
Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen.
Electrophoresis (2003) 24(19-20):3405-20
Cited for: Proteomics
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Malen H, Berven FS, Fladmark KE, Wiker HG,
Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv.
Proteomics (2007) 7(10):1702-18
Cited for: Proteomics
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant